Studies on carboxypeptidase a activity in human serum and its clinical application

1969 ◽  
Vol 4 (2) ◽  
pp. 138-139
Author(s):  
M. Wada ◽  
K. Tsujino ◽  
K. Araki ◽  
T. Saji ◽  
K. Okuda
Keyword(s):  
Human Serum ◽  
Clinical Application ◽  
Carboxypeptidase A

scholarly journals Clinical application and analysis of hepatitis C virus NS3 antigen detection by ELISA in human serum

2007 ◽  
Vol 120 (4) ◽  
pp. 294-299 ◽  
Author(s):  
Li XIE ◽  
Xiao-dong WU ◽  
De-zhuang HUANG ◽  
Hai-lun CHEN ◽  
Li-xiang HE ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Human Serum ◽  
Clinical Application ◽  
Antigen Detection

Assay of Parathyroid Hormone in Human Serum and its Uses

1976 ◽  
Vol 13 (1-6) ◽  
pp. 549-554 ◽  
Author(s):  
J. S. Woodhead ◽  
D. A. Walker
Keyword(s):  
Differential Diagnosis ◽  
Parathyroid Hormone ◽  
Human Serum ◽  
No Value ◽  
Clinical Application ◽  
Calcium Metabolism ◽  
Clinical Problem ◽  
Plasma Calcium ◽  
Biochemical Data ◽  
Health And Disease

The assay of parathyroid hormone has contributed greatly to our understanding of calcium metabolism in health and disease. The most important clinical application of the assay is in the differential diagnosis of hypercalcaemia, which is an increasing clinical problem. PTH assays are of little or no value in the absence of other biochemical data, especially accurate determinations of plasma calcium and phosphate.

A unique activity assay for carboxypeptidase A in human serum

1982 ◽  
Vol 125 (2) ◽  
pp. 420-426 ◽  
Author(s):  
Lynn M. Peterson ◽  
Barton Holmquist ◽  
J.L. Bethune
Keyword(s):  
Human Serum ◽  
Activity Assay ◽  
Carboxypeptidase A

Postsynthetic modification of human enolase isoenzymes.

1987 ◽  
Vol 33 (6) ◽  
pp. 757-760 ◽  
Author(s):  
N R Rigiani ◽  
R A Wevers ◽  
E Rijk ◽  
J B Soons
Keyword(s):  
Activation Energy ◽  
Apparent Activation Energy ◽  
Human Serum ◽  
Original Form ◽  
Carboxypeptidase A ◽  
Activity Profile ◽  
Postsynthetic Modification ◽  
Human Serum Protein ◽  
Energy Gamma ◽  
Gamma Enolase

Abstract The original form of beta beta enolase (EC 4.2.1.11) in tissue is modified to two more electrophoretically distinct forms when incubated with human serum. The three postsynthetic forms are designated beta beta 3, beta beta 2, and beta beta 1, in order of increasing anodal mobility and increasing modification. Serum and carboxypeptidases A and B all produce identical modifications of beta beta enolase but exhibit very different pH-activity profiles. A purified human serum protein previously named "modifying protein," which is responsible for the modification of creatine kinase-M and alpha-enolase subunits, modifies beta beta enolase and also has a pH-activity profile identical to that for serum. Thus we conclude that the modifying protein is not identical to either carboxypeptidase A or B; it may, however, be an as-yet-undescribed carboxypeptidase. With increased modification, both alpha alpha and beta beta enolase decrease in apparent activation energy; gamma gamma enolase shows no evidence of modification, and its apparent activation energy remains stable. Measurement of activation energy is an easy tool for screening for postsynthetic modifications in an enzyme.

A paper-based SERS assay for sensitive duplex cytokine detection towards the atherosclerosis-associated disease diagnosis

2020 ◽  
Vol 8 (16) ◽  
pp. 3582-3589
Author(s):  
Chunxia Li ◽  
Yuan Liu ◽  
Xiaoyan Zhou ◽  
Yuling Wang
Keyword(s):  
Human Serum ◽  
Clinical Application ◽  
Disease Diagnosis ◽  
Sandwich Immunoassay ◽  
Excellent Performance ◽  
Promising Candidate ◽  
Nanoporous Membrane ◽  
Cytokine Detection

Novel SERS based sensing assay was built by combining nanoporous membrane with sandwich immunoassay for duplex cytokines detection. It can be used as a promising candidate for clinical application due to its excellent performance in human serum.

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